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Cryopreservation differentially alters the proteome of epididymal and ejaculated pig spermatozoa

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dc.contributor.authorPerez-Patiño, Cristina
dc.contributor.authorBarranco, Cascales
dc.contributor.authorLi, Junwei
dc.contributor.authorPadilla, Lorena
dc.contributor.authorMartínez, Emilio A
dc.contributor.authorRodriguez-Martinez, Heriberto
dc.contributor.authorRoca, Jordi
dc.contributor.authorParrilla, Inmaculada
dc.contributor.departmentMedicina y Cirugía Animal
dc.date.accessioned2024-02-02T12:38:50Z
dc.date.available2024-02-02T12:38:50Z
dc.date.issued2019-04-11
dc.description© 2019. The authors. This document is made available under the CC-BY 4.0 license http://creativecommons.org/licenses/by /4.0/ This document is the published version of a published work that appeared in final form in International Journal of Molecular Sciences. To access the final work, see DOI: https://doi.org/10.3390/ijms20071791
dc.description.abstractCryopreservation induces differential remodeling of the proteome in mammalian spermatozoa. How these proteome changes relate to the loss of sperm function during cryopreservation remains unsolved. The present study aimed to clarify this issue evaluating differential changes in the proteome of fresh and frozen-thawed pig spermatozoa retrieved from the cauda epididymis and the ejaculate of the same boars, with clear differences in cryotolerance. Spermatozoa were collected from 10 healthy, sexually mature, and fertile boars, and cryopreserved using a standard 0.5 mL-straw protocol. Total and progressive motility, viability, and mitochondria membrane potential were higher and membrane fluidity and reactive oxygen species generation lower in frozen-thawed (FT) epididymal than ejaculated spermatozoa. Quantitative proteomics of fresh and FT spermatozoa were analyzed using a LC-ESI-MS/MS-based Sequential Window Acquisition of All Theoretical Spectra approach. Cryopreservation quantitatively altered more proteins in ejaculated than cauda epididymal spermatozoa. Differential protein-protein networks highlighted a set of proteins quantitatively altered in ejaculated spermatozoa, directly involved in mitochondrial functionality which would explain why ejaculated spermatozoa deteriorate during cryopreservation.es
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dc.identifier.citationInternational Journal of Molecular Sciences. 20(7):1791.
dc.identifier.doihttps://doi.org/10.3390/ijms20071791
dc.identifier.issn1661-6596
dc.identifier.issn1422-0067
dc.identifier.urihttp://hdl.handle.net/10201/138524
dc.languageenges
dc.relationMINECO (Spain), FEDER funds (EU) (AGL2015-69738-R), the Seneca Foundation Murcia, Spain (19892/GERM-15), FORSS (745971), and the Swedish Research Council FORMAS (2017-00946), Stockholm, Swedenes
dc.relation.publisherversionhttps://www.mdpi.com/1422-0067/20/7/1791es
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.rightsAttribution-NonCommercial-NoDerivatives 4.0 Internacional*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/*
dc.subjectCryopreservationes
dc.subjectEpididymis
dc.subjectEjaculate
dc.subjectSpermatozoa
dc.subjectProteomics
dc.subjectPorcine
dc.titleCryopreservation differentially alters the proteome of epididymal and ejaculated pig spermatozoaes
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
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